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Protein

Keratin, type I cytoskeletal 12

Gene

Krt12

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

May play a unique role in maintaining the normal corneal epithelial function. Together with KRT3, essential for the maintenance of corneal epithelium integrity (By similarity).By similarity

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Keratin, type I cytoskeletal 12
Alternative name(s):
Cytokeratin-12
Short name:
CK-12
Keratin-12
Short name:
K12
Type I keratin Ka12
Gene namesi
Name:Krt12By similarity
Synonyms:Ka12Imported, Krt1-12Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1304805. Krt12.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament, Keratin

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Keratin, type I cytoskeletal 12PRO_0000282956Add
BLAST

Proteomic databases

PaxDbiQ6IFW5.
PRIDEiQ6IFW5.

Interactioni

Subunit structurei

Heterotetramer of two type I and two type II keratins. Keratin-3 associates with keratin-12 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016337.

Structurei

3D structure databases

ProteinModelPortaliQ6IFW5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 114114HeadSequence analysisAdd
BLAST
Regioni115 – 397283RodSequence analysisAdd
BLAST
Regioni115 – 15036Coil 1ASequence analysisAdd
BLAST
Regioni154 – 17118Linker 1Sequence analysisAdd
BLAST
Regioni172 – 26392Coil 1BSequence analysisAdd
BLAST
Regioni264 – 28623Linker 12Sequence analysisAdd
BLAST
Regioni287 – 397111Coil 2Sequence analysisAdd
BLAST
Regioni398 – 45659TailSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 11395Gly-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the intermediate filament family.Sequence analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
HOVERGENiHBG013015.
InParanoidiQ6IFW5.
KOiK07604.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 2 hits.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6IFW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSVRTSAL SRRSSSQNGV AGRPWGASAS SVACGYGGTA SGFGVGCGGL
60 70 80 90 100
LSAASMFGSS SGFSGGSTGC SPGLGTAYGG PLGAGVGGMG IGGSSGGGSL
110 120 130 140 150
CIFSGNDGGL LSGSEKETMQ NLNDRLASYL GKVRALEEAN AELENKIREW
160 170 180 190 200
YETRRTGDSG SQSDYSKYYP LIEDLKNKII SASVSNAQLL LQIDNARLAA
210 220 230 240 250
EDFRMKYENE LALRQTVEAD INGLRRVLDE LTLARADLEA QTENLTEELA
260 270 280 290 300
YMKKNHEEEL QSFQAGGPGE VNVEMDAAPG VDLTKSGELR KEINSNTEQL
310 320 330 340 350
QSSKSEVTDL KRMVQNLEIE LQSQLAMKSS LEGSLAETEG GYCCQLSQMQ
360 370 380 390 400
QLIGSLEEQL QQLRADAERQ NEDHQRLLGV KARLEMEIET YRRLLEGDTQ
410 420 430 440 450
GDGFDESLSL TVSKPQAPSV DSSKDPNKTR KIKTVVQEIV NGEVVSSQVQ

ELEEAM
Length:456
Mass (Da):48,820
Last modified:July 5, 2004 - v1
Checksum:i15E5B2653EB3599E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03075828 Genomic DNA. No translation available.
BK004033 mRNA. Translation: DAA04467.1.
RefSeqiNP_001008761.1. NM_001008761.1.
UniGeneiRn.94852.

Genome annotation databases

GeneIDi360625.
KEGGirno:360625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03075828 Genomic DNA. No translation available.
BK004033 mRNA. Translation: DAA04467.1.
RefSeqiNP_001008761.1. NM_001008761.1.
UniGeneiRn.94852.

3D structure databases

ProteinModelPortaliQ6IFW5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016337.

Proteomic databases

PaxDbiQ6IFW5.
PRIDEiQ6IFW5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi360625.
KEGGirno:360625.

Organism-specific databases

CTDi3859.
RGDi1304805. Krt12.

Phylogenomic databases

eggNOGiENOG410IFTF. Eukaryota.
ENOG410Y9IV. LUCA.
HOVERGENiHBG013015.
InParanoidiQ6IFW5.
KOiK07604.

Miscellaneous databases

NextBioi673505.
PROiQ6IFW5.

Family and domain databases

InterProiIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PfamiPF00038. Filament. 2 hits.
[Graphical view]
PRINTSiPR01248. TYPE1KERATIN.
SMARTiSM01391. Filament. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway1 Publication.
  2. "Comprehensive analysis of keratin gene clusters in humans and rodents."
    Hesse M., Zimek A., Weber K., Magin T.M.
    Eur. J. Cell Biol. 83:19-26(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiK1C12_RAT
AccessioniPrimary (citable) accession number: Q6IFW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.